Abstract
Pax5 regulates the B cell-specific expression of the mb-1 gene together with members of the Ets family of transcriptional activators. The Ets proteins on their own bind poorly to the Pax5/Ets binding site, but can be recruited to the site by cooperative interactions with Pax5. The structure of the ETS domain of Ets-1 and the paired domain of Pax5 bound to DNA reveals the molecular details of the selective recruitment of different Ets proteins by Pax5. Comparison with structures of Ets-1 alone bound to both high- and low-affinity DNA sites reveals that Pax5 alters the Ets-1 contacts with DNA. The ability of one protein to alter the DNA sequence-specific contacts of another provides a general mechanism for combinatorial regulation of transcription.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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Crystallography, X-Ray
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DNA / chemistry*
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DNA / genetics
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DNA / metabolism*
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Nucleic Acid Conformation*
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PAX5 Transcription Factor
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Protein Binding
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Protein Structure, Tertiary
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Proteins / chemistry*
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Proteins / metabolism*
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Proto-Oncogene Protein c-ets-1
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Proto-Oncogene Proteins / chemistry*
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-ets
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Substrate Specificity
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Transcription Factors / chemistry*
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Transcription Factors / metabolism*
Substances
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DNA-Binding Proteins
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PAX5 Transcription Factor
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Peptide Fragments
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Proteins
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Proto-Oncogene Protein c-ets-1
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-ets
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Transcription Factors
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DNA
Associated data
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PDB/1K78
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PDB/1K79
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PDB/1K7A